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Co-factor free transaminase

Analyse Co-factor free transaminase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZTX
Type: protein
Length: 859 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transaminase
UniProt: F2XBU9
Pockets: 4 · best druggability 0.88

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transaminase	protein	424	44% helix, 18% strand	F2XBU9
B	Transaminase	protein	435	43% helix, 17% strand	F2XBU9

Ligands and binding sites

EDO · 1,2-ethanediol · additive · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1100	0.88	0.89	111	empty
2	837	0.79	0.82	94	EDO
3	142	0.40	0.73	29	empty
4	83	0.36	0.76	18	empty

Interfaces

1 interface between chains.

A–B · 4000 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

5ZTX · co-factor free Transaminase · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt F2XBU9
Elsewhere: RCSB PDB 5ZTX · PDBe 5ZTX · UniProt F2XBU9

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